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- W2029686885 abstract "We describe a preparative isolation method for a minor chlorophyll a/b protein complex from spinach Photosystem II, which we suggest is identical to the CP29 complex first reported by Machold, O. and Meister, A. (Biochim. Biophys. Acta 546 (1979) 472–480) and by Camm, E.L. and Green, B.R. (Plant Physiol. 66 (1980) 428–432). The CP29 complex was isolated in mg quantities by ion-exchange high-performance liquid chromatography and extensively characterized. The absorption maximum in the red region was at 678 nm. The purified complex retained 10–12 chlorophyll molecules per protein and had a chlorophyll a/b ratio of 3.0–3.2. The complex contained only one apoprotein with an apparent molecular weight between 29 and 31.5 kDa. It showed a fluorescence emission peak at 679 nm when measured at 77 K while the fluorescence excitation spectrum revealed three main peaks in the blue region at 431 nm (chlorophyll a), 468 nm (chlorophyll b) and 493 nm (carotenoids). N-terminal sequencing of fragments from the trypsin-treated CP29 gave a consensus sequence of 29 amino acids." @default.
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- W2029686885 date "1989-12-01" @default.
- W2029686885 modified "2023-09-30" @default.
- W2029686885 title "Isolation and characterization of the chlorophyll a/b protein complex CP29 from spinach" @default.
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- W2029686885 doi "https://doi.org/10.1016/s0005-2728(89)80084-2" @default.
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